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Dual specificity protein phosphatase CDC14A (EC 3.1.3.16) (EC 3.1.3.48) (CDC14 cell division cycle 14 homolog A)

 CC14A_HUMAN             Reviewed;         594 AA.
Q9UNH5; A6MA65; B1AQ14; B1AQ15; O43171; O60727; O60728; Q52LH9;
Q8IXX0;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 147.
RecName: Full=Dual specificity protein phosphatase CDC14A;
EC=3.1.3.16;
EC=3.1.3.48;
AltName: Full=CDC14 cell division cycle 14 homolog A;
Name=CDC14A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=9367992; DOI=10.1074/jbc.272.47.29403;
Li L., Ernsting B.R., Wishart M.J., Lohse D.L., Dixon J.E.;
"A family of putative tumor suppressors is structurally and
functionally conserved in humans and yeast.";
J. Biol. Chem. 272:29403-29406(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10409437; DOI=10.1006/geno.1999.5863;
Wong A.K.C., Chen Y., Lian L., Ha P.C., Petersen K., Laity K.,
Carillo A., Emerson M., Heichman K., Gupte J., Tavtigian S.V.,
Teng D.H.-F.;
"Genomic structure, chromosomal location, and mutation analysis of the
human CDC14A gene.";
Genomics 59:248-251(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
TISSUE=Placenta;
Hao L., Baskerville C., Charbonneau H.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Belyaev A.S., Kolokithas A., Monell C.R.;
"Human CDC14A splice variant.";
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-345 AND PHE-589.
NIEHS SNPs program;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
DEPHOSPHORYLATION OF FZR1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
CYS-278.
PubMed=11598127; DOI=10.1074/jbc.M108126200;
Bembenek J., Yu H.;
"Regulation of the anaphase-promoting complex by the dual specificity
phosphatase human Cdc14a.";
J. Biol. Chem. 276:48237-48242(2001).
[10]
SUBSTRATE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF ASP-251; CYS-278 AND ARG-284.
PubMed=12134069; DOI=10.1091/mbc.01-11-0535;
Kaiser B.K., Zimmerman Z.A., Charbonneau H., Jackson P.K.;
"Disruption of centrosome structure, chromosome segregation, and
cytokinesis by misexpression of human Cdc14A phosphatase.";
Mol. Biol. Cell 13:2289-2300(2002).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF MET-362 AND
ILE-364.
PubMed=11901424; DOI=10.1038/ncb777;
Mailand N., Lukas C., Kaiser B.K., Jackson P.K., Bartek J., Lukas J.;
"Deregulated human Cdc14A phosphatase disrupts centrosome separation
and chromosome segregation.";
Nat. Cell Biol. 4:317-322(2002).
[12]
INTERACTION WITH KIF20A, AND SUBCELLULAR LOCATION.
PubMed=15263015; DOI=10.1083/jcb.200403084;
Gruneberg U., Neef R., Honda R., Nigg E.A., Barr F.A.;
"Relocation of Aurora B from centromeres to the central spindle at the
metaphase to anaphase transition requires MKlp2.";
J. Cell Biol. 166:167-172(2004).
[13]
FUNCTION AS SIRT2 PHOSPHATASE.
PubMed=17488717; DOI=10.1074/jbc.M702990200;
North B.J., Verdin E.;
"Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent
phosphorylation.";
J. Biol. Chem. 282:19546-19555(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND SER-583, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
INVOLVEMENT IN DFNB105.
PubMed=27259055; DOI=10.1016/j.ajhg.2016.04.015;
Delmaghani S., Aghaie A., Bouyacoub Y., El Hachmi H., Bonnet C.,
Riahi Z., Chardenoux S., Perfettini I., Hardelin J.P., Houmeida A.,
Herbomel P., Petit C.;
"Mutations in CDC14A, encoding a protein phosphatase involved in hair
cell ciliogenesis, cause autosomal-recessive severe to profound
deafness.";
Am. J. Hum. Genet. 98:1266-1270(2016).
[16]
VARIANT [LARGE SCALE ANALYSIS] TYR-493.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Dual-specificity phosphatase. Required for centrosome
separation and productive cytokinesis during cell division.
Dephosphorylates SIRT2 around early anaphase. May dephosphorylate
the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent
degradation of mitotic cyclins and subsequent exit from mitosis.
{ECO:0000269|PubMed:11901424, ECO:0000269|PubMed:12134069,
ECO:0000269|PubMed:17488717, ECO:0000269|PubMed:9367992}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- SUBUNIT: Interacts with KIF20A, which is required to localize
CDC14 to the midzone of the mitotic spindle.
{ECO:0000269|PubMed:15263015}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9367992}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:11901424, ECO:0000269|PubMed:12134069}.
Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:11901424, ECO:0000269|PubMed:15263015}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15263015}.
Cell projection, kinocilium {ECO:0000250|UniProtKB:Q6GQT0}.
Note=Centrosomal during interphase, released into the cytoplasm at
the onset of mitosis. Subsequently localizes to the mitotic
spindle pole and at the central spindle (PubMed:12134069,
PubMed:11901424, PubMed:15263015). Present along both the
transient kinocilia of developing cochlear hair cells and the
persistent kinocilia of vestibular hair cells (By similarity).
{ECO:0000250|UniProtKB:Q6GQT0, ECO:0000269|PubMed:11901424,
ECO:0000269|PubMed:12134069, ECO:0000269|PubMed:15263015}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=CDC14A1;
IsoId=Q9UNH5-1; Sequence=Displayed;
Name=2; Synonyms=CDC14A2;
IsoId=Q9UNH5-2; Sequence=VSP_012037;
Name=3; Synonyms=CDC14A3;
IsoId=Q9UNH5-3; Sequence=VSP_012035, VSP_012036;
Name=4; Synonyms=CDC14A4;
IsoId=Q9UNH5-4; Sequence=VSP_012322, VSP_012323;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q9UNH5-5; Sequence=VSP_047597;
-!- DOMAIN: Composed of two structurally equivalent A and B domains
that adopt a dual specificity protein phosphatase (DSP) fold.
{ECO:0000250}.
-!- DISEASE: Deafness, autosomal recessive, 105 (DFNB105)
[MIM:616958]: A form of non-syndromic sensorineural hearing loss.
Sensorineural deafness results from damage to the neural receptors
of the inner ear, the nerve pathways to the brain, or the area of
the brain that receives sound information.
{ECO:0000269|PubMed:27259055}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class CDC14 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB88277.1; Type=Frameshift; Positions=6; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdc14a/";
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EMBL; AF000367; AAB88277.1; ALT_FRAME; mRNA.
EMBL; AF122013; AAD49217.1; -; mRNA.
EMBL; AF064102; AAC16659.1; -; mRNA.
EMBL; AF064103; AAC16660.1; -; mRNA.
EMBL; DQ530256; ABF74568.1; -; mRNA.
EMBL; AY623111; AAT38107.1; -; Genomic_DNA.
EMBL; AL589990; CAH70068.1; -; Genomic_DNA.
EMBL; AC104457; CAH70068.1; JOINED; Genomic_DNA.
EMBL; AL589990; CAH70069.1; -; Genomic_DNA.
EMBL; AC104457; CAH70069.1; JOINED; Genomic_DNA.
EMBL; AL589990; CAH70070.1; -; Genomic_DNA.
EMBL; AC104457; CAH70070.1; JOINED; Genomic_DNA.
EMBL; CH471097; EAW72956.1; -; Genomic_DNA.
EMBL; CH471097; EAW72958.1; -; Genomic_DNA.
EMBL; CH471097; EAW72959.1; -; Genomic_DNA.
EMBL; BC038979; AAH38979.1; -; mRNA.
EMBL; BC093916; AAH93916.1; -; mRNA.
EMBL; BC093918; AAH93918.1; -; mRNA.
CCDS; CCDS769.1; -. [Q9UNH5-1]
CCDS; CCDS770.1; -. [Q9UNH5-2]
CCDS; CCDS771.1; -. [Q9UNH5-3]
RefSeq; NP_001306139.1; NM_001319210.1. [Q9UNH5-5]
RefSeq; NP_001306140.1; NM_001319211.1.
RefSeq; NP_001306141.1; NM_001319212.1.
RefSeq; NP_003663.2; NM_003672.3. [Q9UNH5-1]
RefSeq; NP_201569.1; NM_033312.2. [Q9UNH5-2]
RefSeq; NP_201570.1; NM_033313.2. [Q9UNH5-3]
UniGene; Hs.127411; -.
ProteinModelPortal; Q9UNH5; -.
SMR; Q9UNH5; -.
BioGrid; 114126; 52.
IntAct; Q9UNH5; 1.
MINT; MINT-8330048; -.
STRING; 9606.ENSP00000354916; -.
BindingDB; Q9UNH5; -.
ChEMBL; CHEMBL1772926; -.
DEPOD; Q9UNH5; -.
iPTMnet; Q9UNH5; -.
PhosphoSitePlus; Q9UNH5; -.
BioMuta; CDC14A; -.
DMDM; 55976620; -.
EPD; Q9UNH5; -.
PaxDb; Q9UNH5; -.
PeptideAtlas; Q9UNH5; -.
PRIDE; Q9UNH5; -.
Ensembl; ENST00000336454; ENSP00000336739; ENSG00000079335. [Q9UNH5-1]
Ensembl; ENST00000361544; ENSP00000354916; ENSG00000079335. [Q9UNH5-2]
Ensembl; ENST00000370124; ENSP00000359142; ENSG00000079335. [Q9UNH5-3]
GeneID; 8556; -.
KEGG; hsa:8556; -.
UCSC; uc001dte.5; human. [Q9UNH5-1]
CTD; 8556; -.
DisGeNET; 8556; -.
EuPathDB; HostDB:ENSG00000079335.18; -.
GeneCards; CDC14A; -.
HGNC; HGNC:1718; CDC14A.
HPA; HPA023783; -.
MalaCards; CDC14A; -.
MIM; 603504; gene.
MIM; 616958; phenotype.
neXtProt; NX_Q9UNH5; -.
OpenTargets; ENSG00000079335; -.
PharmGKB; PA26254; -.
eggNOG; KOG1720; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00390000010254; -.
HOGENOM; HOG000198341; -.
HOVERGEN; HBG050818; -.
InParanoid; Q9UNH5; -.
KO; K06639; -.
OMA; LIGACEF; -.
OrthoDB; EOG091G04FM; -.
PhylomeDB; Q9UNH5; -.
TreeFam; TF101053; -.
Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
SIGNOR; Q9UNH5; -.
GeneWiki; CDC14A; -.
GenomeRNAi; 8556; -.
PRO; PR:Q9UNH5; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000079335; -.
CleanEx; HS_CDC14A; -.
ExpressionAtlas; Q9UNH5; baseline and differential.
Genevisible; Q9UNH5; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0060091; C:kinocilium; IEA:UniProtKB-SubCell.
GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0000922; C:spindle pole; IBA:GO_Central.
GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:ProtInc.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
GO; GO:0071850; P:mitotic cell cycle arrest; IBA:GO_Central.
GO; GO:0051256; P:mitotic spindle midzone assembly; IBA:GO_Central.
GO; GO:0007096; P:regulation of exit from mitosis; IBA:GO_Central.
Gene3D; 3.90.190.10; -; 2.
InterPro; IPR029260; DSPn.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR026068; Dual_Pase_CDC14A.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
PANTHER; PTHR23339:SF77; PTHR23339:SF77; 1.
Pfam; PF00782; DSPc; 1.
Pfam; PF14671; DSPn; 1.
SMART; SM00195; DSPc; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF52799; SSF52799; 2.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Deafness; Hydrolase;
Non-syndromic deafness; Nucleus; Phosphoprotein; Polymorphism;
Protein phosphatase; Reference proteome.
CHAIN 1 594 Dual specificity protein phosphatase
CDC14A.
/FTId=PRO_0000094876.
REGION 7 162 A.
REGION 163 176 Linker.
REGION 177 343 B.
ACT_SITE 278 278 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10044}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 583 583 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 174 191 RVENGDFNWIVPGKFLAF -> VILFTPLKPTFLISKSIM
(in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012322.
VAR_SEQ 192 594 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012323.
VAR_SEQ 380 383 DNLE -> VSFP (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.3}.
/FTId=VSP_012035.
VAR_SEQ 384 594 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.3}.
/FTId=VSP_012036.
VAR_SEQ 586 594 SLQSEYVHY -> VSAQTPPPGPQNPECNFCALPSQPRLPP
KKFNSAKEAF (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_012037.
VAR_SEQ 586 594 SLQSEYVHY -> CSCLLLVFRKPFLGSPLLSLPISHL
(in isoform 5). {ECO:0000303|Ref.4}.
/FTId=VSP_047597.
VARIANT 345 345 R -> Q (in dbSNP:rs28364897).
{ECO:0000269|Ref.5}.
/FTId=VAR_019957.
VARIANT 493 493 D -> Y (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035655.
VARIANT 589 589 S -> F (in dbSNP:rs28364923).
{ECO:0000269|Ref.5}.
/FTId=VAR_019958.
MUTAGEN 251 251 D->A: Loss of phosphatase activity.
{ECO:0000269|PubMed:12134069}.
MUTAGEN 278 278 C->S: Loss of phosphatase activity.
{ECO:0000269|PubMed:11598127,
ECO:0000269|PubMed:12134069}.
MUTAGEN 284 284 R->A: Loss of phosphatase activity.
{ECO:0000269|PubMed:12134069}.
MUTAGEN 362 362 M->A: Inappropriate nucleolar
localization; when associated with A-364.
{ECO:0000269|PubMed:11901424}.
MUTAGEN 364 364 I->A: Inappropriate nucleolar
localization; when associated with A-362.
{ECO:0000269|PubMed:11901424}.
CONFLICT 164 164 F -> I (in Ref. 1; AAB88277).
{ECO:0000305}.
CONFLICT 182 182 W -> C (in Ref. 1; AAB88277).
{ECO:0000305}.
SEQUENCE 594 AA; 66574 MW; D5552E2BAEEA84DF CRC64;
MAAESGELIG ACEFMKDRLY FATLRNRPKS TVNTHYFSID EELVYENFYA DFGPLNLAMV
YRYCCKLNKK LKSYSLSRKK IVHYTCFDQR KRANAAFLIG AYAVIYLKKT PEEAYRALLS
GSNPPYLPFR DASFGNCTYN LTILDCLQGI RKGLQHGFFD FETFDVDEYE HYERVENGDF
NWIVPGKFLA FSGPHPKSKI ENGYPLHAPE AYFPYFKKHN VTAVVRLNKK IYEAKRFTDA
GFEHYDLFFI DGSTPSDNIV RRFLNICENT EGAIAVHCKA GLGRTGTLIA CYVMKHYRFT
HAEIIAWIRI CRPGSIIGPQ QHFLEEKQAS LWVQGDIFRS KLKNRPSSEG SINKILSGLD
DMSIGGNLSK TQNMERFGED NLEDDDVEMK NGITQGDKLR ALKSQRQPRT SPSCAFRSDD
TKGHPRAVSQ PFRLSSSLQG SAVTLKTSKM ALSPSATAKR INRTSLSSGA TVRSFSINSR
LASSLGNLNA ATDDPENKKT SSSSKAGFTA SPFTNLLNGS SQPTTRNYPE LNNNQYNRSS
NSNGGNLNSP PGPHSAKTEE HTTILRPSYT GLSSSSARFL SRSIPSLQSE YVHY


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Catalog number Product name Quantity
EIAAB05799 CDC14 cell division cycle 14 homolog A,Cdc14a,Dual specificity protein phosphatase CDC14A,Mouse,Mus musculus
EIAAB05798 CDC14 cell division cycle 14 homolog A,CDC14A,Dual specificity protein phosphatase CDC14A,Homo sapiens,Human
15-288-21523 Dual specificity protein phosphatase CDC14B - EC 3.1.3.48; EC 3.1.3.16; CDC14 cell division cycle 14 homolog B Polyclonal 0.1 mg
15-288-21523 Dual specificity protein phosphatase CDC14B - EC 3.1.3.48; EC 3.1.3.16; CDC14 cell division cycle 14 homolog B Polyclonal 0.05 mg
EIAAB05800 CDC14 cell division cycle 14 homolog B,Cdc14b,Dual specificity protein phosphatase CDC14B,Mouse,Mus musculus
EIAAB05801 CDC14 cell division cycle 14 homolog B,CDC14B,Dual specificity protein phosphatase CDC14B,Homo sapiens,Human
EIAAB05802 CDC14 cell division cycle 14 homolog C,CDC14B2,CDC14C,Dual specificity protein phosphatase CDC14C,Homo sapiens,Human
CDC16 CDC14A Gene CDC14 cell division cycle 14 homolog A (S. cerevisiae)
20-272-190247 Cdc14A - Mouse monoclonal [DCS - 291] to Cdc14A; EC 3.1.3.48; EC 3.1.3.16; CDC14 cell division cycle 14 homolog A Monoclonal 0.05 ml
201-20-0953 CDC14A{Homo sapiens CDC14 cell division cycle 14 homolog }rabbit.pAb 0.1ml
CSB-EL004985MO Mouse CDC14 cell division cycle 14 homolog A (S. cerevisiae) (CDC14A) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL004985HU Human CDC14 cell division cycle 14 homolog A (S. cerevisiae) (CDC14A) ELISA kit, Species Human, Sample Type serum, plasma 96T
CDC20 CDC14B Gene CDC14 cell division cycle 14 homolog B (S. cerevisiae)
20-372-60182 cell division cycle 25 homolog C (S. cerevisiae) (CDC25C) - Mouse monoclonal anti-human CDC25C antibody; EC 3.1.3.48; Dual specificity phosphatase Cdc25C Monoclonal 0.1 mg
GS-0341a Homo sapiens CDC14 cell division cycle 14 homolog primary antibody, Host: Rabbit 200ul
CSB-EL004985MO Mouse Dual specificity protein phosphatase CDC14A(CDC14A) ELISA kit 96T
CSB-EL004985HU Human Dual specificity protein phosphatase CDC14A(CDC14A) ELISA kit 96T
CSB-EL004985MO Mouse Dual specificity protein phosphatase CDC14A(CDC14A) ELISA kit SpeciesMouse 96T
CSB-EL004985HU Human Dual specificity protein phosphatase CDC14A(CDC14A) ELISA kit SpeciesHuman 96T
CC14A_MOUSE ELISA Kit FOR Dual specificity protein phosphatase CDC14A; organism: Mouse; gene name: Cdc14a 96T
CSB-EL004986HU Human CDC14 cell division cycle 14 homolog B (S. cerevisiae) (CDC14B) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL004986MO Mouse CDC14 cell division cycle 14 homolog B (S. cerevisiae) (CDC14B) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL004987HU Human CDC14 cell division cycle 14 homolog C (S. cerevisiae) (CDC14C) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-PA004985GA01HU Rabbit anti-human CDC14 cell division cycle 14 homolog A (S. cerevisiae) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-PA004985GA01HU Rabbit anti-human CDC14 cell division cycle 14 homolog A (S. cerevisiae) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul


 

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